ID   R4X8Z7_TAPDE            Unreviewed;       522 AA.
AC   R4X8Z7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=sphinganine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00038965};
DE            EC=4.1.2.27 {ECO:0000256|ARBA:ARBA00038965};
DE   AltName: Full=Sphingosine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00042568};
GN   ORFNames=TAPDE_000148 {ECO:0000313|EMBL:CCG80622.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG80622.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG80622.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCG80622.1}.
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DR   EMBL; CAHR02000003; CCG80622.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4X8Z7; -.
DR   STRING; 1097556.R4X8Z7; -.
DR   VEuPathDB; FungiDB:TAPDE_000148; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   Proteomes; UP000013776; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 6.10.140.2150; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776}.
FT   MOD_RES         342
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   522 AA;  56812 MW;  FFCBF82283168C3E CRC64;
     MQTLTKVKRS YKKYAGQIQT IRNIYTLYII IKNLLLLSDH IRLYGASGTA SQFYSFVKRV
     AFKAFVSTPG IKGKVQKQVK DALAGLDEKM LPKAGTIRYQ NLPTKGMSKD QLQIELKKLH
     DMGGETDWES GKVSGAIYHG GKDMGELLSS AYSLFSLSNP LHPDVFPGVR KMEAEVVQMV
     LNMFHAPTNG GGTTTSGGTE SILMACKAAR ERGRIEKGIT KPEMIVPITV HAAFDKAASY
     FGITLHHIKV DPITFQVDLS SVERLINKNT VLLAGSAPNF PHGVIDDITS LSALGLRNDI
     PVHVDACLGS FLVPFLEKAG FETPLFDFRL PGVTSISCDT HKYGFAPKGS SVIMYRDRSL
     RKYQYFVSTD WPGGVYASPS IAGSRPGAII AGCWTAMMNM GQDGYIASCK EIVGARVKIQ
     NRIENEIPEL RIIGRPLVSV VAFDSPVVNI YTVGDKMSKL GWHLNGLQTP PALHIACTKL
     TVNAVDTLIA DLKSCVKQVQ EEGGGGDAGS MGKQLPYVQT CN
//